RPAP3 c-terminus. Determined by X-ray diffraction at 1.78 Å resolution. Released 13 Mar 2019.
Explore 6FM8 in 3D Show helices and sheets RCSB PDB PDBe
6FM8 contains 3 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 580-585 | 6 | |
| α-helix | 588-604 | 17 | |
| α-helix | 609-623 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA polymerase II-associated protein 3 | A | protein | 50 | Homo sapiens | Q9H6T3 (AlphaFold model) |
>6FM8_1 RNA polymerase II-associated protein 3 (chains A) SLYPKLFQKNLDPDVFNQIVKILHDFYIEKEKPLLIFEILQRLSELKRFD
RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex. Pal, M., Roe, S.M. Nat Commun (2020). DOI 10.1038/s41467-018-03942-1
Other PDB entries of the same protein (UniProt Q9H6T3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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